UBC15_ARATH
ID UBC15_ARATH Reviewed; 161 AA.
AC P42743; O48952; Q67XR1; Q9MAK4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquitin-conjugating enzyme 15;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 15;
DE AltName: Full=PM42;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa 15;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=UBC15; Synonyms=UBC2-1; OrderedLocusNames=At1g45050;
GN ORFNames=F27F5.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=8219072; DOI=10.1007/bf00029013;
RA Bartling D., Rehling P., Weiler E.W.;
RT "Functional expression and molecular characterization of AtUBC2-1, a novel
RT ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana.";
RL Plant Mol. Biol. 23:387-396(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Yan N., Doelling J., Vierstra R.D.;
RT "A new family of ubiquitin-conjugating enzymes (E2S) AtUBC15/16/17/18 in
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-174(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000269|PubMed:8219072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69157.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X68306; CAA48378.1; -; mRNA.
DR EMBL; AF028338; AAC39324.1; -; Genomic_DNA.
DR EMBL; DQ027029; AAY44855.1; -; mRNA.
DR EMBL; AC007915; AAF69157.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32077.1; -; Genomic_DNA.
DR EMBL; BT026105; ABG48461.1; -; mRNA.
DR EMBL; AK176757; BAD44520.1; -; mRNA.
DR PIR; C96509; C96509.
DR PIR; S39483; S39483.
DR RefSeq; NP_564493.1; NM_103582.4.
DR AlphaFoldDB; P42743; -.
DR SMR; P42743; -.
DR BioGRID; 26297; 3.
DR STRING; 3702.AT1G45050.1; -.
DR PaxDb; P42743; -.
DR PRIDE; P42743; -.
DR ProteomicsDB; 228715; -.
DR EnsemblPlants; AT1G45050.1; AT1G45050.1; AT1G45050.
DR GeneID; 841072; -.
DR Gramene; AT1G45050.1; AT1G45050.1; AT1G45050.
DR KEGG; ath:AT1G45050; -.
DR Araport; AT1G45050; -.
DR TAIR; locus:2028255; AT1G45050.
DR eggNOG; KOG0427; Eukaryota.
DR HOGENOM; CLU_030988_15_1_1; -.
DR InParanoid; P42743; -.
DR OMA; LTEWQIN; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; P42743; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42743; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42743; baseline and differential.
DR Genevisible; P42743; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..161
FT /note="Ubiquitin-conjugating enzyme 15"
FT /id="PRO_0000082575"
FT DOMAIN 15..161
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 99
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 33
FT /note="T -> S (in Ref. 1; CAA48378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18262 MW; 60C7F34A9574FB68 CRC64;
MTSSSAPSRK ALSKIACNRL QKELSEWQLN PPTGFRHKVT DNLQKWTIDV TGAPGTLYAN
ETYQLQVEFP EHYPMEAPQV VFVSPAPSHP HIYSNGHICL DILYDSWSPA MTVNSVCISI
LSMLSSSPAK QRPADNDRYV KNCKNGRSPK ETRWWFHDDK V
